spacer Structure of neuronal nitric oxide synthase heme domain in complex with (R)-1,2-bis((2-amino-4-methylpyridin-6-yl)-methoxy)-propan-3-amine
Accession P29476search
Keywords 3D-structure, Complete proteome, Oxidoreductase, Iron, Metal-binding, Flavoprotein, Cell membrane, NADP, Ubl conjugation, FMN, Membrane, FAD, Heme, Alternative splicing, Calmodulin-binding, Reference proteome, Cell projection, Direct protein sequencing
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Polymers A B
Enzyme nomenclature
EC number ExPASy BRENDA search
Polymers B, A
Name nitric-oxide synthase (NADPH dependent), nitric-oxide synthase
Comment Binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin. This eukaryotic enzyme, which is found in plants and animals [1-3], consists of oxygenase and reductase domains that are linked via a regulatory calmodulin-binding domain. Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center. May produce superoxide under certain conditions. cf. EC, nitric-oxide synthase [NAD(P)H dependent].
The enzyme in brain, but not that induced in lung or liver by endotoxin, requires Ca2+. The stoichiometry is not clear, but may involve a two-electron and a one-electron oxidation step.